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The periciliary ring in polarized epithelial cells is a hot spot for delivery of the apical protein gp135
In polarized epithelial cells, newly synthesized cell surface proteins travel in carrier vesicles from the trans Golgi network to the apical or basolateral plasma membrane. Despite extensive research on polarized trafficking, the sites of protein delivery are not fully characterized. Here we use the...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4621837/ https://www.ncbi.nlm.nih.gov/pubmed/26504168 http://dx.doi.org/10.1083/jcb.201502045 |
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author | Stoops, Emily H. Hull, Michael Olesen, Christina Mistry, Kavita Harder, Jennifer L. Rivera-Molina, Felix Toomre, Derek Caplan, Michael J. |
author_facet | Stoops, Emily H. Hull, Michael Olesen, Christina Mistry, Kavita Harder, Jennifer L. Rivera-Molina, Felix Toomre, Derek Caplan, Michael J. |
author_sort | Stoops, Emily H. |
collection | PubMed |
description | In polarized epithelial cells, newly synthesized cell surface proteins travel in carrier vesicles from the trans Golgi network to the apical or basolateral plasma membrane. Despite extensive research on polarized trafficking, the sites of protein delivery are not fully characterized. Here we use the SNAP tag system to examine the site of delivery of the apical glycoprotein gp135. We show that a cohort of gp135 is delivered to a ring surrounding the base of the primary cilium, followed by microtubule-dependent radial movement away from the cilium. Delivery to the periciliary ring was specific to newly synthesized and not recycling protein. A subset of this newly delivered protein traverses the basolateral membrane en route to the apical membrane. Crumbs3a, another apical protein, was not delivered to the periciliary region, instead making its initial apical appearance in a pattern that resembled its steady-state distribution. Our results demonstrate a surprising “hot spot” for gp135 protein delivery at the base of the primary cilium and suggest the existence of a novel microtubule-based directed movement of a subset of apical surface proteins. |
format | Online Article Text |
id | pubmed-4621837 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-46218372016-04-26 The periciliary ring in polarized epithelial cells is a hot spot for delivery of the apical protein gp135 Stoops, Emily H. Hull, Michael Olesen, Christina Mistry, Kavita Harder, Jennifer L. Rivera-Molina, Felix Toomre, Derek Caplan, Michael J. J Cell Biol Research Articles In polarized epithelial cells, newly synthesized cell surface proteins travel in carrier vesicles from the trans Golgi network to the apical or basolateral plasma membrane. Despite extensive research on polarized trafficking, the sites of protein delivery are not fully characterized. Here we use the SNAP tag system to examine the site of delivery of the apical glycoprotein gp135. We show that a cohort of gp135 is delivered to a ring surrounding the base of the primary cilium, followed by microtubule-dependent radial movement away from the cilium. Delivery to the periciliary ring was specific to newly synthesized and not recycling protein. A subset of this newly delivered protein traverses the basolateral membrane en route to the apical membrane. Crumbs3a, another apical protein, was not delivered to the periciliary region, instead making its initial apical appearance in a pattern that resembled its steady-state distribution. Our results demonstrate a surprising “hot spot” for gp135 protein delivery at the base of the primary cilium and suggest the existence of a novel microtubule-based directed movement of a subset of apical surface proteins. The Rockefeller University Press 2015-10-26 /pmc/articles/PMC4621837/ /pubmed/26504168 http://dx.doi.org/10.1083/jcb.201502045 Text en © 2015 Stoops et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/). |
spellingShingle | Research Articles Stoops, Emily H. Hull, Michael Olesen, Christina Mistry, Kavita Harder, Jennifer L. Rivera-Molina, Felix Toomre, Derek Caplan, Michael J. The periciliary ring in polarized epithelial cells is a hot spot for delivery of the apical protein gp135 |
title | The periciliary ring in polarized epithelial cells is a hot spot for delivery of the apical protein gp135 |
title_full | The periciliary ring in polarized epithelial cells is a hot spot for delivery of the apical protein gp135 |
title_fullStr | The periciliary ring in polarized epithelial cells is a hot spot for delivery of the apical protein gp135 |
title_full_unstemmed | The periciliary ring in polarized epithelial cells is a hot spot for delivery of the apical protein gp135 |
title_short | The periciliary ring in polarized epithelial cells is a hot spot for delivery of the apical protein gp135 |
title_sort | periciliary ring in polarized epithelial cells is a hot spot for delivery of the apical protein gp135 |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4621837/ https://www.ncbi.nlm.nih.gov/pubmed/26504168 http://dx.doi.org/10.1083/jcb.201502045 |
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